P99024 (TBB5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tubulin beta-5 chain

Gene names

Name:

Tubb5

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	444 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.
Subunit structure	Dimer of alpha and beta chains. May interact with RNABP10. Interacts with PIFO. Interacts with MX1 By similarity. Ref.10 Ref.13
Subcellular location	Cytoplasm › cytoskeleton.
Tissue specificity	Ubiquitously expressed with highest levels in spleen, thymus and immature brain.
Post-translational modification	Some glutamate residues at the C-terminus are either polyglutamylated or polyglycylated. These 2 modifications occur exclusively on glutamate residues and result in either polyglutamate or polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of such modifications is still unclear but they are regulate the assembly and dynamics of axonemal microtubules.
Sequence similarities	Belongs to the tubulin family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Microtubule
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	protein folding Traceable author statement. Source: Reactome protein polymerization Inferred from electronic annotation. Source: InterPro spindle assembly Inferred from direct assay PubMed 15121885. Source: MGI
Cellular_component	cell body Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome microtubule Inferred from direct assay PubMed 15121885. Source: MGI nuclear envelope lumen Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay PubMed 18480465. Source: MGI plasma membrane Inferred from electronic annotation. Source: Compara tubulin complex Non-traceable author statement Ref.1. Source: UniProtKB
Molecular_function	GTP binding Non-traceable author statement Ref.1. Source: UniProtKB GTPase activity Inferred from electronic annotation. Source: InterPro structural constituent of cytoskeleton Inferred from direct assay PubMed 15121885. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 444	444	Tubulin beta-5 chain		PRO_0000048246
Regions
	Nucleotide binding	140 – 146	7	GTP Potential
Amino acid modifications
	Modified residue	58	1	N6-acetyllysine By similarity
	Modified residue	172	1	Phosphoserine; by CDK1 By similarity
	Modified residue	318	1	Omega-N-methylarginine By similarity
	Modified residue	340	1	Phosphotyrosine Ref.9 Ref.11
	Modified residue	382	1	Phosphoserine Ref.7
	Cross-link	58		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
	Cross-link	324		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Experimental info
	Sequence conflict	15	1	Q → P in BAB27292. Ref.2
	Sequence conflict	114	1	D → N in BAE40217. Ref.2
	Sequence conflict	143	1	T → N in BAE28709. Ref.2
	Sequence conflict	264	1	H → D in BAE40217. Ref.2
	Sequence conflict	307	1	H → N in BAE39835. Ref.2
	Sequence conflict	357	1	P → T in BAE40217. Ref.2
	Sequence conflict	400	1	G → A in AAA40510. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P99024 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: 1E6CD0A36773A103	FASTA	444	49,671
	10 20 30 40 50 60 MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLDRISVY YNEATGGKYV 70 80 90 100 110 120 PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV 130 140 150 160 170 180 RKEAESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVV PSPKVSDTVV 190 200 210 220 230 240 EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL 250 260 270 280 290 300 RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQVFDAKNMM 310 320 330 340 350 360 AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG 370 380 390 400 410 420 LKMAVTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS 430 440 EYQQYQDATA EEEEDFGEEA EEEA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The mammalian beta-tubulin repertoire: hematopoietic expression of a novel, heterologous beta-tubulin isotype." Wang D., Villasante A., Lewis S.A., Cowan N.J. J. Cell Biol. 103:1903-1910(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and DBA/2. Tissue: Bone marrow, Embryo, Kidney, Liver, Pituitary, Placenta, Spinal ganglion, Spleen, Sympathetic ganglion and Thymus.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 3-19; 63-121; 163-174; 217-241; 242-276; 283-297; 310-318; 321-359 AND 381-390, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain and Hippocampus.
[6]	"Five mouse tubulin isotypes and their regulated expression during development." Lewis S.A., Lee M.G.-S., Cowan N.J. J. Cell Biol. 101:852-861(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 325-444.
[7]	"Quantitative analysis of both protein expression and serine / threonine post-translational modifications through stable isotope labeling with dithiothreitol." Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L., Hart G.W., Burlingame A.L. Proteomics 5:388-398(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[8]	"Tubulin polyglutamylase enzymes are members of the TTL domain protein family." Janke C., Rogowski K., Wloga D., Regnard C., Kajava A.V., Strub J.-M., Temurak N., van Dijk J., Boucher D., van Dorsselaer A., Suryavanshi S., Gaertig J., Edde B. Science 308:1758-1762(2005) [PubMed] [Europe PMC] [Abstract] Cited for: POLYGLUTAMYLATION.
[9]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-340, MASS SPECTROMETRY. Tissue: Mast cell.
[10]	"RanBP10 is a cytoplasmic guanine nucleotide exchange factor that modulates noncentrosomal microtubules." Schulze H., Dose M., Korpal M., Meyer I., Italiano J.E. Jr., Shivdasani R.A. J. Biol. Chem. 283:14109-14119(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RANBP10.
[11]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-340, MASS SPECTROMETRY. Tissue: Brain.
[12]	"Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation." Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C. Cell 137:1076-1087(2009) [PubMed] [Europe PMC] [Abstract] Cited for: POLYGLYCYLATION.
[13]	"Pitchfork regulates primary cilia disassembly and left-right asymmetry." Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B., Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H. Dev. Cell 19:66-77(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PIFO.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X04663 mRNA. Translation: CAA28369.1. AK010960 mRNA. Translation: BAB27292.1. AK011263 mRNA. Translation: BAB27504.1. AK051164 mRNA. Translation: BAC34541.1. AK051393 mRNA. Translation: BAC34623.1. AK083327 mRNA. Translation: BAC38866.1. AK146567 mRNA. Translation: BAE27265.1. AK148978 mRNA. Translation: BAE28709.1. AK151215 mRNA. Translation: BAE30210.1. AK151670 mRNA. Translation: BAE30596.1. AK160225 mRNA. Translation: BAE35700.1. AK161575 mRNA. Translation: BAE36471.1. AK165249 mRNA. Translation: BAE38103.1. AK167691 mRNA. Translation: BAE39738.1. AK167779 mRNA. Translation: BAE39811.1. AK167808 mRNA. Translation: BAE39835.1. AK167926 mRNA. Translation: BAE39931.1. AK168271 mRNA. Translation: BAE40217.1. AK169123 mRNA. Translation: BAE40903.1. AK169210 mRNA. Translation: BAE40982.1. AK169295 mRNA. Translation: BAE41051.1. CR974451 Genomic DNA. Translation: CAO77890.1. BC003825 mRNA. Translation: AAH03825.1. M28732 mRNA. Translation: AAA40510.1.
IPI	IPI00117352.
PIR	E25437.
RefSeq	NP_035785.1. NM_011655.5.
UniGene	Mm.273538. Mm.472638.
3D structure databases
ProteinModelPortal	P99024.
ModBase	Search...
Protein-protein interaction databases
IntAct	P99024. 27 interactions.
PTM databases
PhosphoSite	P99024.
2D gel databases
REPRODUCTION-2DPAGE	IPI00117352. P99024.
SWISS-2DPAGE	P99024.
Proteomic databases
PRIDE	P99024.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000001566; ENSMUSP00000001566; ENSMUSG00000001525.
GeneID	22154.
KEGG	mmu:22154.
Organism-specific databases
CTD	22154.
MGI	MGI:107812. Tubb5.
Phylogenomic databases
GeneTree	ENSGT00700000104169.
HOVERGEN	HBG000089.
InParanoid	B1B178.
KO	K07375.
OMA	RYQGEND.
OrthoDB	EOG4DFPNJ.
Enzyme and pathway databases
Reactome	REACT_17056. Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding. REACT_93132. Metabolism of proteins.
Gene expression databases
ArrayExpress	P99024.
Bgee	P99024.
CleanEx	MM_TUBB5.
Genevestigator	P99024.
GermOnline	ENSMUSG00000001525. Mus musculus.
Family and domain databases
Gene3D	1.10.287.600. 1 hit. 3.30.1330.20. 1 hit. 3.40.50.1440. 1 hit.
InterPro	IPR013838. Beta-tubulin_BS. IPR002453. Beta_tubulin. IPR008280. Tub_FtsZ_C. IPR000217. Tubulin. IPR018316. Tubulin/FtsZ_2-layer-sand-dom. IPR023123. Tubulin_C. IPR017975. Tubulin_CS. IPR003008. Tubulin_FtsZ_GTPase. [Graphical view]
PANTHER	PTHR11588. PTHR11588. 1 hit.
Pfam	PF00091. Tubulin. 1 hit. PF03953. Tubulin_C. 1 hit. [Graphical view]
PRINTS	PR01163. BETATUBULIN. PR01161. TUBULIN.
SMART	SM00864. Tubulin. 1 hit. SM00865. Tubulin_C. 1 hit. [Graphical view]
SUPFAM	SSF55307. Tub_FtsZ_C. 1 hit. SSF52490. Tubulin_FtsZ. 1 hit.
PROSITE	PS00227. TUBULIN. 1 hit. PS00228. TUBULIN_B_AUTOREG. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P99024.
ChiTaRS	TUBB. mouse.
NextBio	302074.
SOURCE	Search...

Entry information

Entry name

TBB5_MOUSE

Accession

Primary (citable) accession number: P99024
Secondary accession number(s): B1B178 , P05218, Q3TFB6, Q3THH9, Q3TIL1, Q3UAV4, Q3UF52, Q8WUC1, Q9CY33

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program